ProductInformation
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD COLLOID (see page 2)
APPEARANCE: Clear dark red liquid
EXTINCTION COEFFICIENT: Certificate of Analysis reports absorbance and gold content of product.
CONCENTRATION: Approximately 0.01% as HAuCl4
STABILITY/STORAGE:
Store at 2-8°C for up to 18 months. Freezing may cause aggregation. Sodium azide (0.02%) has been
added as preservative. Once stabilized with protein, the solution may be supplemented with an
antibacterial agent and stored at 2-8°C.
CERTIFICATE OF ANALYSIS: Lot specific Certificate of Analysis is available.
CHOOSING A PARTICLE SIZE:
Generally, particles <15 nm are most useful in transmission electron microscopy (TEM) and for applications
41
where access to the probe may be hindered by larger particles. Particles >15 nm are more suitable for
scanning electron microscopy (SEM), light microscopy and blotting. Sigma’s gold colloids are all
monodisperse (the coefficient of variance of the particle size is <15% of the mean particle size). In electron
microscopy, monodisperse particles facilitate quantitation and allow for dual labeling with different particle
42
sizes.
GENERAL GUIDELINES FOR USAGE:
The proper pH and concentration must be determined for each protein selected to complex with the
43,44
27
The tannic acid in the gold sol must be broken down to reduce its masking effects. After ligand
gold.
45
adsorption, final blocking of the sol may be done with polyethylene glycol (PEG), BSA or gelatin. After
stabilization of the gold (by reacting with protein), excess ligand should be removed by centrifugation or
44,46
chromatography, and aggregates should be removed by centrifugation.
1
GOLD COLLOIDS AND GOLD CONJUGATES
DESCRIPTION:
Colloidal gold is an electron-dense, non-fading marker useful as a probe in electron microscopy (TEM and
26
SEM), light microscopy and blotting. It requires no additional processing for detection, but in some
4,40
applications the signal can be enhanced by reaction with silver.
It can be complexed with biomolecules
1
by strong, non-covalent interactions. All unconjugated gold colloids offered by Sigma contain about
0.01% HAuCl4 suspended in 0.01% tannic acid with 0.04% trisodium citrate, 0.26 mM potassium carbonate
and 0.02% sodium azide as preservative; all are produced by a modified tannic acid method of Slot and
27
Geuze.
GOLD COLLOIDS
PRODUCT NO.
NAME - DESCRIPTION
PARTICLE SIZE
G-1402
Gold Colloid
Spec: 5 nm
Mean: 3-6 nm
(monodisperse)
G-1527
Gold Colloid
Spec: 10 nm
Mean:8-12 nm
(monodisperse)
G-1652
Gold Colloid
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
2
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD-ANTIBODY CONJUGATES (see page 4)
APPEARANCE: Clear dark red liquid
EXTINCTION COEFFICIENT: Certificate of Analysis reports absorbance and gold content of product.
STABILITY/STORAGE:
Store at 2-8°C for up to 18 months.
Sodium azide (0.05%) has been added as preservative.
CERTIFICATE OF ANALYSIS: Lot specific Certificate of Analysis is available.
CHOOSING A PARTICLE SIZE:
Generally, particles <15 nm are most useful in transmission electron microscopy (TEM) and for applications
41
where access to the probe may be hindered by larger particles. Particles >15 nm are more suitable for
scanning electron microscopy (SEM), light microscopy and blotting. Sigma’s gold colloids are all
monodisperse (the coefficient of variance of the particle size is <15% of the mean particle size). In electron
microscopy, monodisperse particles facilitate quantitation and allow for dual labeling with different particle
42
sizes.
GENERAL GUIDELINES FOR USAGE:
Gold-conjugated antibodies should be diluted for most applications using 0.5 M NaCl buffered at pH 6-8
with 0.1% BSA, 0.05% Tween 20 and 50% fetal bovine serum to minimize background staining. For most
applications dilutions may range from A520=1.0-0.05 (1:5-1:100 dilution), Incubation times range from
0.5-12 hours.
DESCRIPTION:
Gold-antibody conjugates are used to detect antigens and require no additional reagents, unless silver
enhancement is used to increase assay sensitivity. These products are typically used as probes in electron
2,3,4
and light microscopy and immunoblotting procedures.
All antibodies are conjugated to gold by a
1
modification of Geoghagan’s method. Conjugates are tested for immunoreactivity using the dot blot assay
4
of Brada and Roth. These products are supplied as suspensions in 20% glycerol with 1% BSA, 0.02 M Tris
buffered saline, pH 8.0 and 0.05% sodium azide.
3
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD-ANTIBODY CONJUGATES
PRODUCT
NO.
NAME - DESCRIPTION
HOST ANIMAL
G-0786
Affinity Isolated Antibody to Human IgG ( -chain specific)
5 nm colloidal gold labeled (monodisperse)
Antibody adsorbed with mouse serum proteins.
Goat
G-0911
Affinity Isolated Antibody to Human IgM ( -chain specific)
10 nm colloidal cold labeled (monodisperse)
Goat
G-5402
Affinity Isolated Antibody to Goat IgG (whole molecule)
10 nm colloidal gold labeled (monodisperse)
Rabbit
G-5528
Affinity Isolated Antibody to Goat IgG (whole molecule)
5 nm colloidal cold labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Rabbit
G-5527
Affinity Isolated Antibody to Goat IgG (whole molecule)
10 nm colloidal gold labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Rabbit
G-7652
Affinity Isolated Antibody to Mouse IgG (whole molecule)
10 nm colloidal gold labeled (monodisperse)
Goat
G-7527
Affinity Isolated Antibody to Mouse IgG (whole molecule)
5 nm colloidal gold labeled (monodisperse)
Antibody adsorbed with human serum proteins
Goat
G-7777
Affinity Isolated Antibody to Mouse IgG (whole molecule)
10 nm colloidal gold labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Goat
G-5652
Affinity Isolated Antibody to Mouse IgM ( -chain specific)
10 nm colloidal gold labeled (monodisperse)
Goat
G-7402
Affinity Isolated Antibody to Rabbit IgG (whole molecule)
10 nm gold colloid labeled (monodisperse)
Goat
G-7277
Affinity Isolated Antibody to Rabbit IgG (whole molecule)
5 nm gold colloid labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Goat
G-3779
Affinity Isolated Antibody to Rabbit IgG (whole molecule)
10 nm gold colloid labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Goat
G-5410
Affinity Isolated Antibody to Rat IgG (whole molecule)
5 nm gold colloid labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Goat
G-7035
Affinity Isolated Antibody to Rat IgG (whole molecule)
10 nm gold colloid labeled (monodisperse)
Antibody adsorbed with human serum proteins.
Goat
4
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD-LECTIN CONJUGATES (see pages 6,7, and 8)
APPEARANCE: Clear dark red liquid
EXTINCTION COEFFICIENT: Certificate of Analysis reports absorbance and gold content of product.
STABILITY/STORAGE:
Store at -20°C or at 2-8°C (depending on product) for up to 18 months.
Some of the products may be stored undiluted at -20°C, but diluted samples should not be stored below
0°C, since freezing may cause aggregation of the colloid.
Unless otherwise stated in the description of an individual product number, sodium azide (0.02%) has been
added as preservative.
CERTIFICATE OF ANALYSIS: Lot specific Certificate of Analysis is available.
CHOOSING A PARTICLE SIZE:
Generally, particles <15 nm are most useful in transmission electron microscopy (TEM) and for applications
41
where access to the probe may be hindered by larger particles. Particles >15 nm are more suitable for
scanning electron microscopy (SEM), light microscopy and blotting. Sigma’s gold colloids are all
monodisperse (the coefficient of variance of the particle size is <15% of the mean particle size). In electron
microscopy, monodisperse particles facilitate quantitation and allow for dual labeling with different particle
42
sizes.
GENERAL GUIDELINES FOR USAGE:
Gold-conjugated lectins should be diluted for most applications. It is recommended that the diluent buffer
contain 0.15 M saline buffered at pH 6-8, plus 0.5% albumin and 0.05% Tween 20 to minimize background.
Additional buffer supplements may be required for certain applications. Prior to application, allow the
conjugate to equilibrate for at least 20 minutes in lower glycerol content. The optimum concentration of the
conjugate should be determined empirically; a typical range is A520=1.0-0.05 (1:5-1:100 dilution).
Incubation times range from 0.5-12 hours.
DESCRIPTION:
Lectins are proteins or glycoproteins of plant (non-immune) origin that agglutinate cells and/or precipitate
complex carbohydrates. The agglutination activity of these highly specific carbohydrate binding molecules
is usually inhibited by a simple monosaccharide, but for some lectins di-, tri- or polysaccharides are
required. Conjugation does not alter the specificity of the lectin. For gold conjugates, the lectin’s activity is
determined by a dot blot assay using an appropriate glycoprotein. Further general and specific information
9-13
about lectins can be found on pp. 5-6 and in review articles.
5
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD-LECTIN CONJUGATES
PRODUCT
NO.
NAME - DESCRIPTION
PARTICLE SIZE
SUGAR SPECIFICITY
L-1644
Arachis hypogaea (Peanut)
Affinity purified.
Suspension in 50% glycerol with
0.15 M NaCl, 0.01 M sodium phosphate, pH 7.2,
0.02% PEG 20 and 0.02% sodium azide.
Peanut agglutinin (PNA) does not agglutinate normal
human erythrocytes, but strongly agglutinates
neuraminidase treated erythrocytes. PNA has potent
anti-T activity similar to the anti-T antibody in human
28
serum. The lectin can be used to distinguish between
29
human lymphocyte subsets.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
-gal(163)galNAc
5
Concanavalin A (Con A)
From Canavalia ensiformis (Jack bean).
Affinity purified. Prepared from C-7275.
Suspension in 50% glycerol with 0.15 M NaCl,
2+
0.01 M sodium phosphate, pH 6.8, 0.1 mM Ca ,
2+
0.1 mM Mn , 0.02% PEG 20 and 0.02% sodium azide.
Con A is not blood group specific, but has an affinity for
30
terminal -D-mannosyl and -D-glucosyl residues.
2+
2+
30
Ca and Mn ions are required for activity. Con A
dissociates into dimers at or below pH 5.6; it exists as a
tetramer between pH 5.8 and 7.0; above pH 7.0 higher
31
aggregates are formed. Con A exhibits mitogenic
activity which is dependent on its degree of aggregation.
Succinylation results in an active dimeric form which
32
remains a dimer above pH 5.6. Con A is substantially
free of carbohydrate.
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
-man
14
-glc
6
Dolichos biflorus (Horse gram)
Affinity purified.
Suspension in 50% glycerol with 0.15 M NaCl,
0.01 M sodium phosphate, pH 7.2, 0.02% PEG 20 and
0.02% sodium azide.
Dolichos biflorus agglutinin (DBA) has anti-A1 human
blood group specificity, useful for distinguishing
between A1 and A2 blood types. DBA has strong antiCad activity, and has affinity for terminal N-acetyl- -D33,34
galactosaminyl residues.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
7
Glycine max (Soybean)
Affinity purified.
Suspension in 50% glycerol with 0.15 M NaCl,
0.01 M sodium phosphate, pH 7.2, 0.02% PEG 20 and
0.02% sodium azide.
Glycine max agglutinin (SBA) is not blood group
35
specific, but has affinity for N-acetyl-D-galactosamine.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
L-8529
5
L-4645
5
L-3642
L-4643
L-4768
6
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
-galNAc
galNAc
14
14
14
8
L-2765
8
L-4770
8
Helix pomatia (Roman or edible snail)
Affinity purified.Suspension in 50% glycerol with
0.15 M NaCl, 0.01 M sodium phosphate, pH 6.8,
2+
2+
0.1 mM Ca , 0.1 mM Mn , 0.02% PEG 20 and 0.02%
sodium azide.
Helix pomatia agglutinin (HPA) has anti-A human blood
group specificity and has an affinity for terminal N36
acetyl- -D-galactosaminyl residues.
L-2640
7
L-1769
7
L-2144
7
L-1894
7
L-4893
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
galNAc
14
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
14
Lens culinaris (Lentil)
From purified lectin.
Suspension in 50% glycerol with 0.15 M NaCl,
2+
0.01 M sodium phosphate, pH 7.2, 0.1 mM Ca ,
2+
0.1 mM Mn , 0.02% PEG 20 and 0.02% sodium azide.
Lens culinaris agglutinin (LcH) is not blood group
specific. It has affinity for terminal -D-mannosyl and D-glucosyl residues. LcH Is comprised of 2 isomers:
LcH-A and LcH-B; each has a mol. wt. of 49,000. LcH37
A is mitogenic.
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
Triticum vulgaris (Wheat germ)
Affinity purified.
Suspension in 50% glycerol with 0.15 M NaCl,
0.01 M sodium phosphate, pH 7.2, 0.02% PEG 20 and
0.02% sodium azide.
Wheat germ agglutinin (WGA) is not blood group
specific, but has an affinity for N-acetyl- -Dglucosaminyl residues and N-acetyl- -D-glucosamine
oligomers. WGA contains no protein-bound
38
carbohydrate.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
(glcNAc)2
Ulex europaeus (Gorse or Furze) UEA I
Affinity purified.
Suspension in 50% glycerol with 0.15 M NaCl,
0.01 M sodium phosphate, pH 7.2, 0.02% PEG 20 and
0.02% sodium azide.
Ulex europaeus agglutinin (UEA) has anti-H blood
group specificity. There are 2 types of lectin: UEA I has
affinity for L-fucose and UEA II has affinity for N,N’diacetylchitobiose. The mol. wt. of UEA I was initially
found to be 170,000, but later reports indicate that UEA
I may form aggregates at neutral and basic pH, and that
39
the mol. Wt. is 68,000.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
-L-fuc
14
(glcNAc)2
7
-man
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
14
NeuNAc
14,47
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD-CONJUGATES OF OTHER PROTEINS (see pages 10,11, and 12)
APPEARANCE: Clear dark red liquid
EXTINCTION COEFFICIENT: Certificate of Analysis reports absorbance and gold content of product.
STABILITY/STORAGE:
Store at -20°C or at 2-8°C (depending on product) for up to 18 months.
Some of the products may be stored undiluted at -20°C, but diluted samples should not be stored below
0°C, since freezing may cause aggregation of the colloid.
Unless otherwise stated in the description of an individual product number, sodium azide (0.02%) has been
added as preservative.
CERTIFICATE OF ANALYSIS: Lot specific Certificate of Analysis is available.
CHOOSING A PARTICLE SIZE:
Generally, particles <15 nm are most useful in transmission electron microscopy (TEM) and for applications
41
where access to the probe may be hindered by larger particles. Particles >15 nm are more suitable for
scanning electron microscopy (SEM), light microscopy and blotting. Sigma’s gold colloids are all
monodisperse (the coefficient of variance of the particle size is <15% of the mean particle size). In electron
microscopy, monodisperse particles facilitate quantitation and allow for dual labeling with different particle
42
sizes.
GENERAL GUIDELINES FOR USAGE:
Gold-conjugated proteins should be diluted for most applications. It is recommended that the diluent buffer
contain 0.15 M saline buffered at pH 6-8, plus 0.5% albumin and 0.05% Tween 20 to minimize background.
Additional buffer supplements may be required for certain applications. Prior to application, allow the
conjugate to equilibrate for at least 20 minutes in lower glycerol content. The optimum concentration of the
conjugate should be determined empirically; a typical range is A520=1.0-0.05 (1:5-1:100 dilution).
Incubation times range from 0.5-12 hours.
DESCRIPTION:
Gold conjugates are processed, after adsorption with proteins, to remove free protein and large
4,42
aggregates. The concentration is expressed as absorbance at the absorption maximum (A520).
8
GOLD COLLOIDS AND GOLD CONJUGATES
GOLD CONJUGATES OF OTHER PROTEINS
PRODUCT NO.
A-5179
A-5547
A-4292
A-4417
NAME - DESCRIPTION
PARTICLE SIZE
Albumin Gold Labeled
Bovine albumin (A-0281) adsorbed to colloidal gold. Suitable for use
as a control.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M Tris, pH 7.6,
0.02% PEG 20 and 0.02% sodium azide.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Albumin-Biotin Gold Labeled
Biotinamidocaproyl labeled bovine albumin (A-6043) adsorbed to
colloidal gold. Useful in detection of biotinylated compounds using
15
streptavidin as bridging protein.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M sodium
phosphate, pH 7.4,
0.02% PEG 20 and 0.02% sodium azide.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
E-4259
ExtrAvidin Gold Labeled
ExtrAvidin, a uniquely modified avidin reagent, combines the high
specific activity and sensitivity of avidin with the low background staining
of streptavidin. ExtrAvidin conjugates may be used in conjunction with
biotinylated reagents in the avidin/biotin labeling system.
Suspension in 0.15 M NaCl, 0.01 M TRIS, pH 7.4, 0.02% PEG 20,
0.02% Sodium Azide
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
H-9516
Heparin-Albumin Gold Labeled
Heparin covalently linked to albumin as carrier, adsorbed to colloidal
gold for detection of heparin-bonding compounds.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M sodium
phosphate, pH 7.0, 0.02% PEG 20 and 0.02% sodium azide.
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
H-3278
Heparin-Albumin Gold Labeled
Heparin covalently linked to albumin as a carrier, adsorbed to colloidal
gold for detection of heparin-binding compounds.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M BES, pH 7.2,
0.02% PEG 20 and 0.02% sodium azide.
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
L-3647
Lactoferrin Gold Labeled
Lactoferrin from bovine colostrum (L-4765) coupled through spacer to
18
albumin coated colloidal gold. Particularly useful in detection of DNA.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M BES, pH 7.0,
0.25% BSA and 0.02% sodium azide.
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
H-5641
9
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
P-0304
P-0429
P-1062
P-1187
Peroxidase Gold Labeled
Horseradish peroxidase (P-8375) coupled through spacer to albumin
19
coated colloidal gold.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M MES, pH 6.5,
0.25% BSA. No sodium azide is added because it inhibits peroxidase
activity.
Phosphodiesterase 3’:5’-Cyclic-Nucleotide Activator
(Calmodulin) Gold Labeled
Calmodulin from bovine brain (P-2277) coupled through PEG (M.W.
3350) spacer to albumin coated colloidal gold for the enhanced
20
detection of calmodulin binding compounds.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M BES, pH 7.0,
0.02% PEG 20 and 0.02% sodium azide.
P-1039
Protein A Gold Labeled
21
Extracellular Protein A (P-6031) adsorbed to colloidal gold.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M sodium
phosphate, pH 7.4,
0.02% PEG 20 and 0.02% sodium azide.
P-9785
P-1546
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
P-1312
P-9660
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
Protein G Gold Labeled
22,23
Protein G (P-9659) adsorbed to colloidal gold.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M Tris, pH 7.4,
0.02% PEG 20 and 0.02% sodium azide.
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
P-1671
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
P-1796
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
S-4275
Streptavidin-Albumin Gold Labeled
Streptavidin (S-4762) coupled through spacer to albumin coated
15,24
colloidal gold for enhanced detection of biotinylated compounds.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M BES, pH 7.4,
0.25% BSA and 0.02% sodium azide.
10
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
S-2390
Streptavidin Gold Labeled
24
Streptavidin (S-4762) adsorbed to colloidal gold.
Suspension in 50% glycerol with 0.15 M NaCl, 0.01 M phosphate
buffer, pH 7.4, 0.02% PEG 20 and 0.02% sodium azide.
Spec: 5 nm
Mean: 3.5-6.5 nm
(monodisperse)
S-1139
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
S-6514
Spec: 20 nm
Mean: 17-23 nm
(monodisperse)
T-2654
Trypsin Inhibitor Gold Labeled
Trypsin inhibitor (ovomucoid) from chicken egg white
25
(T-2011) adsorbed to colloidal gold.
Suspension in 40% glycerol with 0.15 M NaCl, 0.01 M potassium
phosphate, pH 7.2, 0.02% PEG 20 and 0.02% sodium azide.
11
Spec: 10 nm
Mean: 8-12 nm
(monodisperse)
GOLD COLLOIDS AND GOLD CONJUGATES
REFERENCES:
1.
2.
3.
4
5.
6.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
W.D. Geoghegan et al., Immunol. Comm., 7, 1 (1978).
M. Horisberger, Biol. Cell., 36, 253 (1979).
J.M. Lucocq and J. Roth, J. Histochem. Cytochem., 30, 691 (1984).
D. Brada and J. Roth, Anal. Biochem., 142, 79 (1984).
N. Benhamou and G. B. Ouellette, J. Histochem. Cytochem., 34, 855 (1986).
J.M. Lucocq and J. Roth, Techniques in Immunocytochemistry, Vol. 3, p. 203, Bullock and Petrusz,
Eds., Academic Press (1985).
M. Horisberger, Techniques in Immunocytochemistry, Vol. 3, p. 155, Bullock and Petrusz, Eds.,
Academic Press (1985).
D. Brown and L. Orci, J. Histochem. Cytochem., 34, 1057 (1986).
E.R. Gold and P. Balding, Receptor-Specific Proteins: Plant and Animal Lectins, Excerpta Medica,
Amsterdam (1975).
J. Roth, The Lectins: Molecular Probes in Cell Biology and Membrane Research, Exp. Pathol. (Sup.
3), Gustav Fischer Verlag, Jena (1978).
Lectins: Biology, Biochemistry, Clinical Biochemistry, T.C. Bog-Hansen, Ed., W. deGruyter, Berlin,
Vols. 1, 2, 3, 4, 5 (1980, 1981, 1982, 1985, 1986).
Lectins: Biology, Biochemistry, Clinical Biochemistry, T.C. Bog-Hansen, et al., Eds., Sigma Chemical
Co., St. Louis, MO, Vols. 6, 7 (1988, 1989).
The Lectins: Properties, Functions and Applications in Biology and Medicine, I. E. Liener, et al., Eds.,
Academic Press, London (1986).
KEY TO SUGAR SPECIFICITY:
-gal(163)galNAc: 2-acetamido-2-deoxy-3-O- -D-galactopyranosyl-D-galactopyranose
-man:
-D-mannose
-glc:
-D-glucose
galNAc: N-acetyl-D-galactosamine
(glcNAc)2:
N-acetyl-D-glucosamine dimer
NeuNAc: N-acetylneuraminic acid
-L-fuc:
-L-fucose
C. Bonnard et al., Immunolabeling for Electron Microscopy, p. 95, Polak and Varndell, Eds., Elsevier
Science Publishers (1984).
J. Roth et al., J. Histochem. Cytochem., 32, 1167 (1984).
B.A. Sela et al., J. Biol. Chem., 250, 7533 (1975).
N. Benhamou, J. Electron. Micr. Tech., 12, 1 (1989).
A.I. Basbaum, J. Histochem. Cytochem., 37, 1811 (1989).
K. Fujimoto et al., J. Histochem. Cytochem., 37, 249 (1989).
M. Horisberger and M.F. Clerk, Histochem., 82, 219 (1985).
M. J. Bendayan, J. Electron. Micr. Tech., 6, 7 (1987).
M. Bendayan and S. Gavzon, J. Histochem. Cytochem., 6, 597 (1988).
P. Liesi et al., J. Histochem. Cytochem., 34, 923 (1986).
W.D. Geoghegan and G. A. Ackermann, J. Histochem. Cytochem., 31, 1394 (1983).
J.E. Beesley, Proc. Royal Micr. Soc., 20, 187 (1985).
J.W. Slot and H.J. Geuze, Eur. J. Cell Biol., 38, 87 (1985).
G.W.G. Bird, Vox Sang., 9, 748 (1964).
J. London et al., J. Immunol., 121, 438 (1978).
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12
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13